P51797 (CLCN6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Chloride transport protein 6

Alternative name(s):
Chloride channel protein 6
Short name=ClC-6

Gene names

Name:	CLCN6
Synonyms:	KIAA0046

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	869 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Chloride transport protein, initially identified as voltage-gated chloride channel. The presence of the conserved gating glutamate residues suggests that is functions as antiporter.
Subcellular location	Endosome membrane; Multi-pass membrane protein. Note: Detected in detergent-resistant lipid rafts. Ref.11
Tissue specificity	Testis, ovary, small intestine, brain and skeletal muscle. Low level expression in aortic and coronary vascular smooth muscle cells, and aortic endothelial cells. Isoform C is only detected in kidney. Ref.1 Ref.2 Ref.10
Post-translational modification	N-glycosylated on several asparagine residues. Ref.11
Miscellaneous	The CLC channel family contains both chloride channels and proton-coupled anion transporters that exchange chloride or another anion for protons. The presence of conserved gating glutamate residues is typical for family members that function as antiporters By similarity.
Sequence similarities	Belongs to the chloride channel (TC 2.A.49) family. ClC-6/CLCN6 subfamily. [View classification] Contains 2 CBS domains.

Ontologies

Keywords
Biological process	Antiport Ion transport Transport
Cellular component	Endosome Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	CBS domain Repeat Transmembrane Transmembrane helix
Ligand	ATP-binding Chloride Nucleotide-binding
PTM	Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell volume homeostasis Non-traceable author statement Ref.1Ref.2. Source: UniProtKB signal transduction Non-traceable author statement Ref.1Ref.2. Source: UniProtKB
Cellular_component	endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Non-traceable author statement Ref.1Ref.2. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW antiporter activity Inferred from electronic annotation. Source: UniProtKB-KW voltage-gated chloride channel activity Non-traceable author statement Ref.1Ref.2. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform A (identifier: P51797-1)

Also known as: Clc-6a;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform B (identifier: P51797-2)

Also known as: ClC-6b; D2-A1;

The sequence of this isoform differs from the canonical sequence as follows:
     237-320: DKRDFVSAGA...LLNFGEFKCS → YGKRQERLCI...APWIAELWRV
     321-869: Missing.

Isoform C (identifier: P51797-3)

Also known as: ClC-6c; D1-A1;

The sequence of this isoform differs from the canonical sequence as follows:
     319-353: CSDSDKKCHLWTAMDLGFFVVMGVIGGLLGATFNC → SLREPPCVSGNHRGGVCGLDGVRRMPTDVLFESNR
     354-869: Missing.

Isoform D (identifier: P51797-4)

Also known as: ClC-6d; D1-A2;

The sequence of this isoform differs from the canonical sequence as follows:
     237-308: DKRDFVSAGA...QFGSWGSFQL → SGCWSCCSFR...APWIAELWRV
     309-869: Missing.

Isoform E (identifier: P51797-5)

The sequence of this isoform differs from the canonical sequence as follows:
     844-869: IVGIITRHNLTYEFLQARLRQHYQTI → VSEAPALPPP...LHLRRDLRIR

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 869	869	Chloride transport protein 6		PRO_0000094449
Regions
	Topological domain	1 – 80	80	Cytoplasmic By similarity
	Transmembrane	81 – 113	33	Helical; By similarity
	Transmembrane	128 – 150	23	Helical; By similarity
	Intramembrane	159 – 166	8	Helical; By similarity
	Transmembrane	176 – 194	19	Helical; By similarity
	Transmembrane	200 – 217	18	Helical; By similarity
	Intramembrane	241 – 253	13	Helical; By similarity
	Intramembrane	257 – 265	9	Helical; By similarity
	Transmembrane	277 – 294	18	Helical; By similarity
	Transmembrane	335 – 364	30	Helical; By similarity
	Transmembrane	371 – 392	22	Helical; By similarity
	Transmembrane	462 – 481	20	Helical; By similarity
	Transmembrane	487 – 511	25	Helical; By similarity
	Intramembrane	519 – 533	15	Helical; By similarity
	Intramembrane	534 – 536	3	Note=Loop between two helices; By similarity
	Intramembrane	537 – 548	12	Helical; By similarity
	Intramembrane	549 – 552	4	Note=Loop between two helices; By similarity
	Transmembrane	553 – 571	19	Helical; By similarity
	Topological domain	572 – 869	298	Cytoplasmic By similarity
	Domain	605 – 662	58	CBS 1
	Domain	807 – 868	62	CBS 2
	Nucleotide binding	630 – 632	3	ATP By similarity
	Nucleotide binding	849 – 852	4	ATP By similarity
	Motif	156 – 160	5	Selectivity filter part_1 By similarity
	Motif	198 – 202	5	Selectivity filter part_2 By similarity
	Motif	487 – 491	5	Selectivity filter part_3 By similarity
	Compositional bias	4 – 18	15	Cys-rich
Sites
	Binding site	157	1	Chloride By similarity
	Binding site	489	1	Chloride; via amide nitrogen By similarity
	Binding site	576	1	Chloride By similarity
	Site	200	1	Mediates proton transfer from the outer aqueous phase to the interior of the protein; involved in linking H(+) and Cl(-) transport By similarity
	Site	267	1	Mediates proton transfer from the protein to the inner aqueous phase By similarity
Amino acid modifications
	Glycosylation	410	1	N-linked (GlcNAc...)
	Glycosylation	422	1	N-linked (GlcNAc...)
	Glycosylation	432	1	N-linked (GlcNAc...)
Natural variations
	Alternative sequence	237 – 320	84	DKRDF…EFKCS → YGKRQERLCISRSGCWSCCS FRGANRGYLVQSRGGFVLLE PRAHVESALLFHVCHLHPQL LPFWDSVWKLGFLPAPWIAE LWRV in isoform B.		VSP_001043
	Alternative sequence	237 – 308	72	DKRDF…GSFQL → SGCWSCCSFRGANRGYLVQS RGGFVLLEPRAHVESALLFH VCHLHPQLLPFWDSVWKLGF LPAPWIAELWRV in isoform D.		VSP_001047
	Alternative sequence	309 – 869	561	Missing in isoform D.		VSP_001048
	Alternative sequence	319 – 353	35	CSDSD…ATFNC → SLREPPCVSGNHRGGVCGLD GVRRMPTDVLFESNR in isoform C.		VSP_001045
	Alternative sequence	321 – 869	549	Missing in isoform B.		VSP_001044
	Alternative sequence	354 – 869	516	Missing in isoform C.		VSP_001046
	Alternative sequence	844 – 869	26	IVGII…HYQTI → VSEAPALPPPLREDPLARCC LCTQASHQKRRHPTRRGECG PTLALNPARLPCTRDPFPCL PADGTSVPLAVLSSQSRAST RLCLPPEMLLFTPYHWCSLV LHLRRDLRIR in isoform E.		VSP_017188
	Natural variant	198	1	E → G. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6 Ref.8 Ref.9 Corresponds to variant rs198400 [ dbSNP | Ensembl ].		VAR_023051
Experimental info
	Mutagenesis	410	1	N → A: Abolishes N-glycosylation; when associated with A-422 and A-432. Ref.11
	Mutagenesis	422	1	N → A: Abolishes N-glycosylation; when associated with A-410 and A-432. Ref.11
	Mutagenesis	432	1	N → A: Abolishes N-glycosylation; when associated with A-410 and A-422. Ref.11

Sequences

	Sequence		Length	Mass (Da)
	Isoform A (Clc-6a) [UniParc]. Last modified November 2, 2010. Version 2. Checksum: D625F0C2189EB6F7	FASTA	869	97,289
	10 20 30 40 50 60 MAGCRGSLCC CCRWCCCCGE RETRTPEELT ILGETQEEED EILPRKDYES LDYDRCINDP 70 80 90 100 110 120 YLEVLETMDN KKGRRYEAVK WMVVFAIGVC TGLVGLFVDF FVRLFTQLKF GVVQTSVEEC 130 140 150 160 170 180 SQKGCLALSL LELLGFNLTF VFLASLLVLI EPVAAGSGIP EVKCYLNGVK VPGIVRLRTL 190 200 210 220 230 240 LCKVLGVLFS VAGGLFVEKE GPMIHSGSVV GAGLPQFQSI SLRKIQFNFP YFRSDRDKRD 250 260 270 280 290 300 FVSAGAAAGV AAAFGAPIGG TLFSLEEGSS FWNQGLTWKV LFCSMSATFT LNFFRSGIQF 310 320 330 340 350 360 GSWGSFQLPG LLNFGEFKCS DSDKKCHLWT AMDLGFFVVM GVIGGLLGAT FNCLNKRLAK 370 380 390 400 410 420 YRMRNVHPKP KLVRVLESLL VSLVTTVVVF VASMVLGECR QMSSSSQIGN DSFQLQVTED 430 440 450 460 470 480 VNSSIKTFFC PNDTYNDMAT LFFNPQESAI LQLFHQDGTF SPVTLALFFV LYFLLACWTY 490 500 510 520 530 540 GISVPSGLFV PSLLCGAAFG RLVANVLKSY IGLGHIYSGT FALIGAAAFL GGVVRMTISL 550 560 570 580 590 600 TVILIESTNE ITYGLPIMVT LMVAKWTGDF FNKGIYDIHV GLRGVPLLEW ETEVEMDKLR 610 620 630 640 650 660 ASDIMEPNLT YVYPHTRIQS LVSILRTTVH HAFPVVTENR GNEKEFMKGN QLISNNIKFK 670 680 690 700 710 720 KSSILTRAGE QRKRSQSMKS YPSSELRNMC DEHIASEEPA EKEDLLQQML ERRYTPYPNL 730 740 750 760 770 780 YPDQSPSEDW TMEERFRPLT FHGLILRSQL VTLLVRGVCY SESQSSASQP RLSYAEMAED 790 800 810 820 830 840 YPRYPDIHDL DLTLLNPRMI VDVTPYMNPS PFTVSPNTHV SQVFNLFRTM GLRHLPVVNA 850 860 VGEIVGIITR HNLTYEFLQA RLRQHYQTI
	Isoform B (ClC-6b) (D2-A1) [UniParc]. Checksum: 68604EBB1B15E8CA	FASTA	320	36,006
	10 20 30 40 50 60 MAGCRGSLCC CCRWCCCCGE RETRTPEELT ILGETQEEED EILPRKDYES LDYDRCINDP 70 80 90 100 110 120 YLEVLETMDN KKGRRYEAVK WMVVFAIGVC TGLVGLFVDF FVRLFTQLKF GVVQTSVEEC 130 140 150 160 170 180 SQKGCLALSL LELLGFNLTF VFLASLLVLI EPVAAGSGIP EVKCYLNGVK VPGIVRLRTL 190 200 210 220 230 240 LCKVLGVLFS VAGGLFVEKE GPMIHSGSVV GAGLPQFQSI SLRKIQFNFP YFRSDRYGKR 250 260 270 280 290 300 QERLCISRSG CWSCCSFRGA NRGYLVQSRG GFVLLEPRAH VESALLFHVC HLHPQLLPFW 310 320 DSVWKLGFLP APWIAELWRV
	Isoform C (ClC-6c) (D1-A1) [UniParc]. Checksum: 078D3E8A2C013E94	FASTA	353	38,814
	10 20 30 40 50 60 MAGCRGSLCC CCRWCCCCGE RETRTPEELT ILGETQEEED EILPRKDYES LDYDRCINDP 70 80 90 100 110 120 YLEVLETMDN KKGRRYEAVK WMVVFAIGVC TGLVGLFVDF FVRLFTQLKF GVVQTSVEEC 130 140 150 160 170 180 SQKGCLALSL LELLGFNLTF VFLASLLVLI EPVAAGSGIP EVKCYLNGVK VPGIVRLRTL 190 200 210 220 230 240 LCKVLGVLFS VAGGLFVEKE GPMIHSGSVV GAGLPQFQSI SLRKIQFNFP YFRSDRDKRD 250 260 270 280 290 300 FVSAGAAAGV AAAFGAPIGG TLFSLEEGSS FWNQGLTWKV LFCSMSATFT LNFFRSGIQF 310 320 330 340 350 GSWGSFQLPG LLNFGEFKSL REPPCVSGNH RGGVCGLDGV RRMPTDVLFE SNR
	Isoform D (ClC-6d) (D1-A2) [UniParc]. Checksum: 60C3293CAC95D6BE	FASTA	308	34,515
	10 20 30 40 50 60 MAGCRGSLCC CCRWCCCCGE RETRTPEELT ILGETQEEED EILPRKDYES LDYDRCINDP 70 80 90 100 110 120 YLEVLETMDN KKGRRYEAVK WMVVFAIGVC TGLVGLFVDF FVRLFTQLKF GVVQTSVEEC 130 140 150 160 170 180 SQKGCLALSL LELLGFNLTF VFLASLLVLI EPVAAGSGIP EVKCYLNGVK VPGIVRLRTL 190 200 210 220 230 240 LCKVLGVLFS VAGGLFVEKE GPMIHSGSVV GAGLPQFQSI SLRKIQFNFP YFRSDRSGCW 250 260 270 280 290 300 SCCSFRGANR GYLVQSRGGF VLLEPRAHVE SALLFHVCHL HPQLLPFWDS VWKLGFLPAP WIAELWRV
	Isoform E [UniParc]. Checksum: 5503065172532131	FASTA	953	106,376
	10 20 30 40 50 60 MAGCRGSLCC CCRWCCCCGE RETRTPEELT ILGETQEEED EILPRKDYES LDYDRCINDP 70 80 90 100 110 120 YLEVLETMDN KKGRRYEAVK WMVVFAIGVC TGLVGLFVDF FVRLFTQLKF GVVQTSVEEC 130 140 150 160 170 180 SQKGCLALSL LELLGFNLTF VFLASLLVLI EPVAAGSGIP EVKCYLNGVK VPGIVRLRTL 190 200 210 220 230 240 LCKVLGVLFS VAGGLFVEKE GPMIHSGSVV GAGLPQFQSI SLRKIQFNFP YFRSDRDKRD 250 260 270 280 290 300 FVSAGAAAGV AAAFGAPIGG TLFSLEEGSS FWNQGLTWKV LFCSMSATFT LNFFRSGIQF 310 320 330 340 350 360 GSWGSFQLPG LLNFGEFKCS DSDKKCHLWT AMDLGFFVVM GVIGGLLGAT FNCLNKRLAK 370 380 390 400 410 420 YRMRNVHPKP KLVRVLESLL VSLVTTVVVF VASMVLGECR QMSSSSQIGN DSFQLQVTED 430 440 450 460 470 480 VNSSIKTFFC PNDTYNDMAT LFFNPQESAI LQLFHQDGTF SPVTLALFFV LYFLLACWTY 490 500 510 520 530 540 GISVPSGLFV PSLLCGAAFG RLVANVLKSY IGLGHIYSGT FALIGAAAFL GGVVRMTISL 550 560 570 580 590 600 TVILIESTNE ITYGLPIMVT LMVAKWTGDF FNKGIYDIHV GLRGVPLLEW ETEVEMDKLR 610 620 630 640 650 660 ASDIMEPNLT YVYPHTRIQS LVSILRTTVH HAFPVVTENR GNEKEFMKGN QLISNNIKFK 670 680 690 700 710 720 KSSILTRAGE QRKRSQSMKS YPSSELRNMC DEHIASEEPA EKEDLLQQML ERRYTPYPNL 730 740 750 760 770 780 YPDQSPSEDW TMEERFRPLT FHGLILRSQL VTLLVRGVCY SESQSSASQP RLSYAEMAED 790 800 810 820 830 840 YPRYPDIHDL DLTLLNPRMI VDVTPYMNPS PFTVSPNTHV SQVFNLFRTM GLRHLPVVNA 850 860 870 880 890 900 VGEVSEAPAL PPPLREDPLA RCCLCTQASH QKRRHPTRRG ECGPTLALNP ARLPCTRDPF 910 920 930 940 950 PCLPADGTSV PLAVLSSQSR ASTRLCLPPE MLLFTPYHWC SLVLHLRRDL RIR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"ClC-6 and ClC-7 are two novel broadly expressed members of the CLC chloride channel family." Brandt S., Jentsch T.J. FEBS Lett. 377:15-20(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), TISSUE SPECIFICITY, VARIANT GLY-198. Tissue: Brain.
[2]	"Alternative splicing of ClC-6 (a member of the ClC chloride-channel family) transcripts generates three truncated isoforms one of which, ClC-6c, is kidney-specific." Eggermont J., Buyse G., Voets T., Tytgat J., De Smedt H., Droogmans G., Nilius B. Biochem. J. 325:269-276(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS B; C AND D), NUCLEOTIDE SEQUENCE [MRNA] OF 1-409 (ISOFORM A), TISSUE SPECIFICITY, VARIANT GLY-198. Tissue: Chronic myeloid leukemia cell.
[3]	"Complete genomic structure of the CLCN6 and CLCN7 putative chloride channel genes." Kornak U., Boesl M.R., Kubisch C. Biochim. Biophys. Acta 1447:100-106(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM A), VARIANT GLY-198.
[4]	"Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1." Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S. DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), VARIANT GLY-198. Tissue: Bone marrow.
[5]	"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones." Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T. DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION.
[6]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), VARIANT GLY-198. Tissue: Hippocampus.
[7]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLY-198.
[9]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A), VARIANT GLY-198. Tissue: Brain.
[10]	"Expression of CLCN voltage-gated chloride channel genes in human blood vessels." Lamb F.S., Clayton G.H., Liu B.-X., Smith R.L., Barna T.J., Schutte B.C. J. Mol. Cell. Cardiol. 31:657-666(1999) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY. Tissue: Aortic endothelium and Vascular smooth muscle.
[11]	"Human ClC-6 is a late endosomal glycoprotein that associates with detergent-resistant lipid domains." Ignoul S., Simaels J., Hermans D., Annaert W., Eggermont J. PLoS ONE 2:E474-E474(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION, MUTAGENESIS OF ASN-410; ASN-422 AND ASN-432.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X83378 mRNA. Translation: CAA58292.1. X96391 mRNA. Translation: CAA65255.1. X99472 Genomic DNA. Translation: CAA67835.1. X99473 mRNA. Translation: CAA67836.1. X99474 mRNA. Translation: CAA67837.1. X99475 mRNA. Translation: CAA67838.1. AF009257 , AF009247, AF009248, AF009249, AF009250, AF009251, AF009252, AF009253, AF009254, AF009255, AF009256 Genomic DNA. Translation: AAB69287.1. D28475 mRNA. Translation: BAA05836.4. AK289999 mRNA. Translation: BAF82688.1. AL953897, AL021155 Genomic DNA. Translation: CAI15891.1. AL953897, AL021155 Genomic DNA. Translation: CAI15892.1. AL953897, AL021155 Genomic DNA. Translation: CAI15893.1. AL953897, AL021155 Genomic DNA. Translation: CAI15894.1. AL953897, AL021155 Genomic DNA. Translation: CAI15895.1. AL021155, AL953897 Genomic DNA. Translation: CAI23402.1. AL021155, AL953897 Genomic DNA. Translation: CAI23403.1. AL021155, AL953897 Genomic DNA. Translation: CAI23404.1. AL021155, AL953897 Genomic DNA. Translation: CAI23405.1. AL021155, AL953897 Genomic DNA. Translation: CAI23406.1. CH471130 Genomic DNA. Translation: EAW71715.1. BC117420 mRNA. Translation: AAI17421.1. BC117424 mRNA. Translation: AAI17425.1.
IPI	IPI00180121. IPI00305252. IPI00395741. IPI00414669. IPI00642888.
PIR	S68428.
RefSeq	NP_001277.1. NM_001286.3.
UniGene	Hs.193043.
3D structure databases
ProteinModelPortal	P51797.
SMR	P51797. Positions 87-639.
ModBase	Search...
PTM databases
PhosphoSite	P51797.
Polymorphism databases
DMDM	311033364.
Proteomic databases
PaxDb	P51797.
PRIDE	P51797.
Protocols and materials databases
DNASU	1185.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000312413; ENSP00000308367; ENSG00000011021. ENST00000346436; ENSP00000234488; ENSG00000011021. ENST00000376496; ENSP00000365679; ENSG00000011021.
GeneID	1185.
KEGG	hsa:1185.
UCSC	uc001ate.4. human. uc009vnf.1. human. uc009vng.1. human. uc009vnh.1. human.
Organism-specific databases
CTD	1185.
GeneCards	GC01P011866.
HGNC	HGNC:2024. CLCN6.
HPA	HPA032097.
MIM	602726. gene.
neXtProt	NX_P51797.
PharmGKB	PA26551.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0038.
HOVERGEN	HBG050985.
KO	K05015.
OMA	TEVEMDK.
OrthoDB	EOG4N5VW7.
PhylomeDB	P51797.
Gene expression databases
ArrayExpress	P51797.
Bgee	P51797.
Genevestigator	P51797.
Family and domain databases
Gene3D	1.10.3080.10. 2 hits.
InterPro	IPR014743. Cl-channel_core. IPR001807. Cl-channel_volt-gated. IPR002248. Cl_channel-6. IPR000644. Cysta_beta_synth_core. [Graphical view]
Pfam	PF00571. CBS. 2 hits. PF00654. Voltage_CLC. 1 hit. [Graphical view]
PRINTS	PR00762. CLCHANNEL. PR01117. CLCHANNEL6.
SMART	SM00116. CBS. 2 hits. [Graphical view]
SUPFAM	SSF81340. Cl-channel_core. 1 hit.
PROSITE	PS51371. CBS. 2 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CLCN6. human.
GenomeRNAi	1185.
NextBio	4898.
SOURCE	Search...

Entry information

Entry name

CLCN6_HUMAN

Accession

Primary (citable) accession number: P51797
Secondary accession number(s): A8K1T4 , O60818, O60819, O60820, O60821, P78520, P78521, Q17R81, Q5SNW2, Q5SNW3, Q5SNX1, Q5SNX2, Q5SNX3, Q99427, Q99428, Q99429

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	November 2, 2010
Last modified:	May 1, 2013
This is version 121 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.